ID S7TGQ2_9BACT Unreviewed; 634 AA.
AC S7TGQ2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 28-JAN-2026, entry version 51.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=dsat_1869 {ECO:0000313|EMBL:EPR35765.1};
OS Alkalidesulfovibrio alkalitolerans DSM 16529.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfovibrionaceae; Alkalidesulfovibrio.
OX NCBI_TaxID=1121439 {ECO:0000313|EMBL:EPR35765.1, ECO:0000313|Proteomes:UP000014975};
RN [1] {ECO:0000313|EMBL:EPR35765.1, ECO:0000313|Proteomes:UP000014975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16529 {ECO:0000313|EMBL:EPR35765.1,
RC ECO:0000313|Proteomes:UP000014975};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
CC -!- FUNCTION: Translation factor necessary for the incorporation of
CC selenocysteine into proteins. It probably replaces EF-Tu for the
CC insertion of selenocysteine directed by the UGA codon. SelB binds GTP
CC and GDP. {ECO:0000256|ARBA:ARBA00025526}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPR35765.1}.
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DR EMBL; ATHI01000002; EPR35765.1; -; Genomic_DNA.
DR RefSeq; WP_020885755.1; NZ_ATHI01000002.1.
DR AlphaFoldDB; S7TGQ2; -.
DR STRING; 1121439.dsat_1869; -.
DR PATRIC; fig|1121439.3.peg.255; -.
DR eggNOG; COG3276; Bacteria.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000014975; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR CDD; cd04171; SelB; 1.
DR CDD; cd03696; SelB_II; 1.
DR CDD; cd15491; selB_III; 1.
DR FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 1.
DR Gene3D; 1.10.10.2770; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR057335; Beta-barrel_SelB.
DR InterPro; IPR050055; EF-Tu_GTPase.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004535; Transl_elong_SelB.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00475; selB; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF25461; Beta-barrel_SelB; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; WHD_2nd_SelB; 1.
DR Pfam; PF09107; WHD_3rd_SelB; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 3.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:EPR35765.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000014975}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 634 AA; 69687 MW; CF15E3CAC4850DCC CRC64;
MAVIMGTAGH IDHGKTSLVR ALTGIDCDRL AEEKRRGITI ELGFAYLDLP DGQRVGVVDV
PGHERFVKNM VAGAAGIDFV MLVIAADEGV MPQTREHLEI CSLLGTATGL VALTKIDAVD
EEWRELVSED VREFLRGTFL EGAPLVPVSS VNGEGVARLR QEIMDIVKAH KARRRSDLTR
LPVDRVFTMK GYGTVITGTL TSGAVDVGDD LVVYPTGIPV KVRSLQSHGA SVQRVEAGRR
TAVNVSGAEV EDISRGDVLA PQGALFPSQV WDARVTLLSS MQKPFKHRKQ VHFHHGSREV
MARVYLLDRD ELAPGESAPA QIRFEEPLTG VFGDHFVMRS HSPLRTIGGG VVLGPYQRKF
KRRSVQAARL SSLPQATPEE LTLFQLEMAG TAGLSFARLL VATNLESKTL EKVLSDLGGR
QQALMFDREE RAYVAGSVVD ELRRGILDHL AAFHRREPLR QGLTRGELAS GFSKTLPQKL
VHFLVERLVR KNEIVQEQEI LRLPGHKVSL ASDQAKAREA VMAAYVKGGI TPPNLKDVLD
PLGLDAKAAA SLFKMLVEQG ELVKVKEDMF FAAGAVESLV ARITEWFATN DDLTPASLRD
LTGLSRKYAI PVLEWLDKEK ITVRVGDKRL LRKR
//
